Search results for "DOMAINS"

showing 10 items of 269 documents

Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE

2017

17 p.-8 fig.

0301 basic medicineProtein ConformationDimerlcsh:MedicineMolecular DynamicsCrystallography X-RayPhysical ChemistryBiochemistryDEAD-box RNA HelicasesMolecular dynamicschemistry.chemical_compoundComputational ChemistryNucleophileBiochemical Simulationslcsh:ScienceMultidisciplinaryCrystallographyChemistryOrganic CompoundsPhysicsEscherichia coli ProteinsCondensed Matter Physics3. Good healthPhysical sciencesChemistryCarbon-Sulfur LyasesBiochemistryCrystal StructureResearch ArticleChemical ElementsProtein subunitChemical physicschemistry.chemical_elementOxidative phosphorylationMolecular Dynamics Simulation03 medical and health sciencesThiolsEscherichia coliSolid State PhysicsProtein Interaction Domains and MotifsChemical BondingOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesComputational BiologyDimers (Chemical physics)Hydrogen BondingCell BiologySulfurAcceptorRedox sensitiveOxidative Stress030104 developmental biologyBiophysicslcsh:QProtein MultimerizationSulfur
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The C-terminal Domains of Apoptotic BH3-only Proteins Mediate Their Insertion into Distinct Biological Membranes

2016

Changes in the equilibrium of pro- and anti-apoptotic members of the B-cell lymphoma-2 (Bcl-2) protein family in the mitochondrial outer membrane (MOM) induce structural changes that commit cells to apoptosis. Bcl-2 homology-3 (BH3)-only proteins participate in this process by either activating pro-apoptotic effectors or inhibiting anti-apoptotic components and by promoting MOM permeabilization. The association of BH3-only proteins with MOMs is necessary for the activation and amplification of death signals; however, the nature of this association remains controversial, as these proteins lack a canonical transmembrane sequence. Here we used an in vitro expression system to study the inserti…

0301 basic medicineProtein familyCèl·lulesBiologyBiochemistryMitochondrial Proteins03 medical and health sciencesProtein DomainsMembranes (Biologia)Protein-fragment complementation assayMembrane BiologyMicrosomesProto-Oncogene ProteinsHumansMolecular BiologyAdaptor Proteins Signal TransducingGeneticsBcl-2-Like Protein 11030102 biochemistry & molecular biologyCell MembraneBcl-2 familyProteïnes de membranaMembrane ProteinsBiological membraneCell BiologyFusion proteinTransmembrane proteinCell biology030104 developmental biologyMembraneProto-Oncogene Proteins c-bcl-2Membrane proteinB-cell lymphoma 2 (Bcl-2) family BH3-only apoptosis membrane insertion membrane protein mitochondrial apoptosis transmembrane domainApoptosis Regulatory ProteinsHydrophobic and Hydrophilic InteractionsHeLa CellsJournal of Biological Chemistry
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Mcl-1 and Bok transmembrane domains : Unexpected players in the modulation of apoptosis

2020

The Bcl-2 protein family comprises both proand antiapoptotic members that control the permeabilization of the mitochondrial outer membrane, a crucial step in the modulation of apoptosis. Recent research has demonstrated that the carboxyl-terminal transmembrane domain (TMD) of some Bcl-2 protein family mem-bers can modulate apoptosis; however, the transmembrane interactome of the antiapoptotic protein Mcl-1 remains largely unexplored. Here, we demonstrate that the Mcl-1 TMD forms homooligomers in the mitochondrial membrane, competes with full-length Mcl-1 protein with regards to its antiapoptotic function, and induces cell death in a Bok-dependent manner. While the Bok TMD oligomers locate p…

0301 basic medicineProtein familyMitochondrionBCL-X(L)Endoplasmic ReticulumInteractome114 Physical sciences03 medical and health sciencesBok0302 clinical medicineProtein DomainsMITOCHONDRIAhemic and lymphatic diseasesAnimalsHumansBcl-2Inner mitochondrial membraneMultidisciplinaryCell DeathChemistryEndoplasmic reticulumapoptosisMcl-1PATHWAYSLOCALIZATIONBiological SciencesTransmembrane protein3. Good healthCell biologytransmembraneTransmembrane domainstomatognathic diseasesGLYCOPHORIN-A DIMERIZATION030104 developmental biologyHELIX PACKINGProto-Oncogene Proteins c-bcl-2BAX030220 oncology & carcinogenesisMitochondrial MembranesPROSURVIVAL BCL-2 PROTEINSMOTIFSURVIVALMyeloid Cell Leukemia Sequence 1 Protein1182 Biochemistry cell and molecular biologyBacterial outer membraneHeLa Cells
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Skeletal organic matrices in molluscs: origin, evolution, diagenesis

2017

8 pages; International audience; The mollusc shell comprises a small amount of organic macromolecules, mostly proteins and polysaccharides, which, all together, constitute the skeletal organic matrix (SOM). In the recent years, the study of the SOM of about two dozens of mollusc species via transcriptomics and/or proteomics has led to the identification of hundreds of shell-associated proteins. This rapidly growing set of data allows several comparisons, shedding light on similarities and differences at the primary structure level and on some peculiar evolutionary mechanisms that may have affected SOM proteins. In addition, it constitutes a prerequisite for investigating the SOM repertoires…

0301 basic medicineProteomicsSubfossilProteinBiologyFunctional domainsProteomicsbiology.organism_classificationFossilizationSequencesTridacnaDiagenesisDiagenesis[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]03 medical and health sciences030104 developmental biology0302 clinical medicineOrder (biology)Evolutionary biologyMollusc shellShellIdentification (biology)14. Life underwaterMollusc030217 neurology & neurosurgery
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Endogenous β-neurexins on axons and within synapses show regulated dynamic behavior

2021

Summary: Neurexins are key organizer molecules that regulate synaptic function and are implicated in autism and schizophrenia. β-neurexins interact with numerous cell adhesion and receptor molecules, but their neuronal localization remains elusive. Using single-molecule tracking and high-resolution microscopy to detect neurexin1β and neurexin3β in primary hippocampal neurons from knockin mice, we demonstrate that endogenous β-neurexins are present in fewer than half of excitatory and inhibitory synapses. Moreover, we observe a large extrasynaptic pool of β-neurexins on axons and show that axonal β-neurexins diffuse with higher surface mobility than those transiently confined within synapses…

0301 basic medicineQH301-705.5Green Fluorescent ProteinsNerve Tissue ProteinsEndogenyHippocampal formationNeurotransmissionGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicineProtein DomainsAnimalsPremovement neuronal activityneurotransmissionBiology (General)synaptic functionCell adhesionelectron microscopyintegumentary systemChemistryCell MembranefungiGlutamate receptorcell adhesionproteaseAxonsCell biologyMice Inbred C57BL030104 developmental biologyEctodomainProteolysisSynapsesExcitatory postsynaptic potentialsingle-particle tracking030217 neurology & neurosurgeryCell Reports
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Interaction between ROR1 and MuSK activation complex in myogenic cells

2017

The ROR family of receptor tyrosine kinases, ROR1 and ROR2, is known to play an important role during skeletal muscle regeneration. ROR1 has a critical role in regulating satellite cell (SC) proliferation during muscle regeneration, and proinflammatory cytokines such as TNF-α and IL-1β can induce expression of ROR1 in myogenic cells via NF-κB activation. While searching for ROR1-interacting proteins in myogenic cells, we identified MuSK as a ROR1-binding protein. MuSK interacts with and phosphorylates ROR1 at the cytoplasmic proline-rich domain. ROR1 also interacts with the MuSK activator Dok-7 independently of MuSK interaction. Collectively, our results identified ROR1 as a new interacting…

0301 basic medicineSatellite Cells Skeletal MuscleBiophysicsMuscle ProteinsReceptor Tyrosine Kinase-like Orphan ReceptorsBiochemistryReceptor tyrosine kinaseCell LineProinflammatory cytokineMice03 medical and health sciencesProtein DomainsStructural BiologyChlorocebus aethiopsGeneticsAnimalsHumansReceptors CholinergicProtein phosphorylationPhosphorylationMolecular BiologyCell ProliferationBinding SitesbiologyKinaseChemistryActivator (genetics)Receptor Protein-Tyrosine KinasesCell DifferentiationROR2Cell BiologyCell biologyHEK293 Cells030104 developmental biologyCOS CellsROR1biology.proteinPhosphorylationProtein BindingFEBS Letters
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On the origin of BAG(3) and its consequences for an expansion of BAG3's role in protein homeostasis

2021

The B-cell CLL 2-associated athanogene (BAG) protein family in general and BAG3, in particular, are pivotal elements of cellular protein homeostasis, with BAG3 playing a major role in macroautophagy. In particular, in the contexts of senescence and degeneration, BAG3 has exhibited an essential role often related to its capabilities to organize and remove aggregated proteins. Exciting studies in different species ranging from human, murine, zebrafish, and plant samples have delivered vital insights into BAG3s' (and other BAG proteins') functions and their regulations. However, so far no studies have addressed neither BAG3's evolution nor its phylogenetic position in the BAG family.

0301 basic medicineSenescenceProteasome Endopeptidase ComplexProtein family610 MedizinBiologyProtein HomeostasisBAG3BiochemistryEvolution MolecularWW domain03 medical and health sciences0302 clinical medicineProtein Domains610 Medical sciencesAutophagyAnimalsHumansMolecular BiologyZebrafishCellular SenescencePhylogenyAdaptor Proteins Signal TransducingAutophagyFungiCell BiologyPlantsbiology.organism_classificationCell biology030104 developmental biologyProteostasis030220 oncology & carcinogenesisProteolysisProteostasisbiology.proteinApoptosis Regulatory ProteinsSignal TransductionJournal of Cellular Biochemistry
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Bronchial inflammation and bacterial load in stable COPD is associated with TLR4 overexpression.

2017

Toll-like receptors (TLRs) and nucleotide-binding oligomerisation domain (NOD)-like receptors (NLRs) are two major forms of innate immune sensors but their role in the immunopathology of stable chronic obstructive pulmonary disease (COPD) is incompletely studied. Our objective here was to investigate TLR and NLR signalling pathways in the bronchial mucosa in stable COPD.Using immunohistochemistry, the expression levels of TLR2, TLR4, TLR9, NOD1, NOD2, CD14, myeloid differentiation primary response gene 88 (MyD88), Toll-interleukin-1 receptor domain-containing adaptor protein (TIRAP), and the interleukin-1 receptor-associated kinases phospho-IRAK1 and IRAK4 were measured in the bronchial muc…

0301 basic medicineTIRAPMaleRespiratory SystemVital CapacityHAEMOPHILUS-INFLUENZAELUNG MICROBIOMEPathogenesisPulmonary Disease Chronic Obstructive0302 clinical medicineNOD2ImmunopathologyForced Expiratory VolumeNod1 Signaling Adaptor ProteinNOD1PhosphorylationCOPDSmoking11 Medical And Health SciencesMiddle AgedCPG-DNAbronchial inflammationAnti-Bacterial AgentsStreptococcus pneumoniaePseudomonas aeruginosaMOUSE LUNGFemaleLife Sciences & BiomedicineMoraxella catarrhalisSignal TransductionEXPRESSIONPulmonary and Respiratory MedicineCD14BronchiRespiratory MucosaReal-Time Polymerase Chain ReactionOBSTRUCTIVE PULMONARY-DISEASETLRs NLR bronchial inflammationNLRDENDRITIC CELL SUBSETS03 medical and health sciencesProtein DomainsmedicineHumansTLRsAgedTOLL-LIKE RECEPTORSCOPD TLR4InflammationScience & TechnologyBacteriabusiness.industrymedicine.diseaseHaemophilus influenzaeBacterial Loadrespiratory tract diseasesToll-Like Receptor 4TLR2030104 developmental biology030228 respiratory systemImmunologyINNATE IMMUNITYT-CELLSbusinessThe European respiratory journal
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2-methoxyestradiol impacts on amino acids-mediated metabolic reprogramming in osteosarcoma cells by interaction with NMDA receptor

2017

Deregulation of serine and glycine metabolism, have been identified to function as metabolic regulators in supporting tumor cell growth. The role of serine and glycine in regulation of cancer cell proliferation is complicated, dependent on concentrations of amino acids and tissue-specific. D-serine and glycine are coagonists of N-methyl-D-aspartate receptor subunit GRIN1. Importantly, NMDA receptors are widely expressed in cancer cells and play an important role in regulation of cell death, proliferation and metabolism of numerous malignancies. The aim of the present work was to associate the metabolism of glycine and D-serine with the anticancer activity of 2-methoxyestradiol. 2-methoxyest…

0301 basic medicineTime Factors2-methoxyestradiol neuronal nitric oxide synthase D-serine glycine osteosarcomaPhysiologyClinical BiochemistryNitric Oxide Synthase Type ISerine0302 clinical medicineCell MovementSerinechemistry.chemical_classificationMembrane Potential MitochondrialOsteosarcomaEstradiolTubulin ModulatorsAmino acidMolecular Docking Simulation030220 oncology & carcinogenesisMCF-7 CellsNMDA receptorOsteosarcomaFemalemedicine.drugProtein BindingSignal TransductionProgrammed cell deathGlycineAntineoplastic AgentsBone NeoplasmsBreast NeoplasmsNerve Tissue ProteinsBiologyMolecular Dynamics SimulationReceptors N-Methyl-D-Aspartate03 medical and health sciencesStructure-Activity RelationshipProtein DomainsmedicineHumans2-MethoxyestradiolCell ProliferationBinding SitesDose-Response Relationship DrugCell BiologyMetabolismmedicine.disease2-Methoxyestradiol030104 developmental biologychemistryCancer cellCancer researchEnergy Metabolism
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Structural and mechanistic insights into the interaction of the circadian transcription factor BMAL1 with the KIX domain of the CREB-binding protein

2019

JBC papers in press xx, 16604-16619 (2019). doi:10.1074/jbc.RA119.009845

0301 basic medicineendocrine systemCircadian clockTranscription factor complex610BiochemistryProtein Structure SecondaryProtein–protein interaction03 medical and health sciencesTransactivationMiceProto-Oncogene Proteins c-mybProtein DomainsX-Ray DiffractionCircadian ClocksScattering Small AngleAnimalsddc:610Amino Acid SequenceCREB-binding proteinMolecular BiologyTernary complexTranscription factorBinding Sites030102 biochemistry & molecular biologybiologyChemistryARNTL Transcription FactorsCell BiologyHistone-Lysine N-MethyltransferaseSurface Plasmon ResonanceCREB-Binding ProteinRecombinant ProteinsCell biologyProtein Structure Tertiary030104 developmental biologyStructural biologyProtein Structure and Foldingbiology.proteinMutagenesis Site-DirectedMyeloid-Lymphoid Leukemia ProteinProtein Binding
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